Research workbench
Studies on the nitroreductase prodrug-activating system. crystal structures of the enzyme active form and complexes with the inhibitor dicoumarol and dinitrobenzamide prodrugs
Analyse Studies on the nitroreductase prodrug-activating system. crystal structures of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OO5
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxygen-insensitive NAD(P)H nitroreductase
- EC
- 1.6.99.7
- UniProt
- P38489
- Ligands
- FMN
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Oxygen-insensitive NAD(P)H nitroreductase (EC 1.6.99.7) | protein | 217 | 54% helix, 15% strand | P38489 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 392 | 0.75 | 0.85 | 42 | FMN |
| 2 | 394 | 0.73 | 0.84 | 44 | FMN |
| 3 | 183 | 0.51 | 0.77 | 22 | empty |
| 4 | 186 | 0.51 | 0.77 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 3784 Ų buried · 64 hydrogen bonds · protein-protein
Compared structures
- 1OO5 · Studies on the Nitroreductase Prodrug-Activating System. Crystal Structures of the Enzyme… · the same entry in another collection · chain A against A, TM-score 1.00
- P38489 · AlphaFold monomer V2.0 prediction for oxygen-insensitive NAD(P)H nitroreductase (P38489) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P38489
- Elsewhere: RCSB PDB 1OO5 · PDBe 1OO5 · UniProt P38489
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